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Terminal sequences of lysosome solubilized pig liver cytochrome b5 reductase
dc.contributor.authorCrabb, John W.en_US
dc.contributor.authorTarr, George E.en_US
dc.contributor.authorYasunobu, Kerry T.en_US
dc.contributor.authorIyanagi, Takashien_US
dc.contributor.authorCoon, Minor J.en_US
dc.date.accessioned2006-04-07T17:22:13Z
dc.date.available2006-04-07T17:22:13Z
dc.date.issued1980-08-29en_US
dc.identifier.citationCrabb, John W., Tarr, George E., Yasunobu, Kerry T., Iyanagi, Takashi, Coon, Minor J. (1980/08/29)."Terminal sequences of lysosome solubilized pig liver cytochrome b5 reductase." Biochemical and Biophysical Research Communications 95(4): 1650-1655. <http://hdl.handle.net/2027.42/23164>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4G3D7X0-1C/2/11b34f1d8d1e307d7e5defd18fc2eb27en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/23164
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7417338&dopt=citationen_US
dc.description.abstractSummaryLysosome solubilized pig liver cytochrome b5 reductase has the following twenty residues as NH2-terminal sequence: Ser-Thr-Pro-Ala-Ile-Thr-Leu-Glu-Asn-Pro-Asp-Ile-Lys-Tyr-Pro-Leu-Arg-Leu-Ile-Asp. The fragment is predicted to exist largely in the random conformation with 2 [beta]-bends at residues 9-12 and 14-17. The reductase fragment appears clean enough for complete sequence investigation and is very similar to cathepsin D-solubilized rabbit liver cytochrome b5 reductase.en_US
dc.format.extent563268 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleTerminal sequences of lysosome solubilized pig liver cytochrome b5 reductaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry Medical School, University of Michigan Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry and Biophysics John A. Burns Medical School, University of Hawaii Honolulu, Hawaii 96822, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry and Biophysics John A. Burns Medical School, University of Hawaii Honolulu, Hawaii 96822, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry and Biophysics John A. Burns Medical School, University of Hawaii Honolulu, Hawaii 96822, USAen_US
dc.contributor.affiliationotherDivision of Biochemistry Tsukuba University School of Medicine Ibaraki 305, Japanen_US
dc.identifier.pmid7417338en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/23164/1/0000089.pdfen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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